The DOI matches its Crossref record; 53 of the 54 references it cites were found in a registry or an index.
Phospholipase Cγ2 Is Essential in the Functions of B Cell and Several Fc Receptors
Open accessAbstract
Many receptors activate phospholipase Cgamma1 or -gamma2. To assess the role of PLCgamma2, we derived enzyme-deficient mice. The mice are viable but have decreased mature B cells, a block in pro-B cell differentiation, and B1 B cell deficiency. IgM receptor-induced Ca2+ flux and proliferation to B cell mitogens are absent. IgM, IgG2a, and IgG3 levels are reduced, and T cell-independent antibody production is absent. The similarity to Btk- or Blnk-deficient mice demonstrates that PLCgamma2 is downstream in Btk/Blnk signaling. FcRgamma signaling is also defective, resulting in a loss of collagen-induced platelet aggregation, mast cell FcepsilonR function, and NK cell FcgammaRIII and 2B4 function. The results define a signal transduction pathway broadly utilized by immunoglobulin superfamily receptors.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“In fact, a previous study reported marked decreases in the most mature B cell population in Plcg2 deficient mice(30).”
From Multi-omics analyses reveal novel effects of PLCγ2 deficiency in the mouse brain (2023) · cites this paper as [30]
In the citing paper
“Previous studies have reported internal hemorrhaging during development in other Plcg2 deficient mouse models (29, 30), which have been proposed to be caused by rupture of blood-filled fragile lymphatic vessels by mechanical stress or pressure of the blood flow (29).”
From Multi-omics analyses reveal novel effects of PLCγ2 deficiency in the mouse brain (2023) · cites this paper as [30]
In the citing paper
“PLCγ2 is primarily expressed in lymphoid tissue (bone marrow, thymus, spleen and lymph nodes), where it functions immediately downstream of the B-cell receptor (BCR) and other ITAM-coupled receptors [22–24].”
From PLCγ2 deficiency compromises systemic immune tolerance and erodes myelin homeostasis while enhancing oxidative metabolism in the mouse brain (2026) · cites this paper as [22]
In the citing paper
“In peripheral immune cells, PLCγ2 has been implicated in signaling pathways downstream of the B cell receptor, and it is thought to modulate the functions of macrophages, platelets, mast cells, neutrophils, and NK cells through the Fc receptor [14].”
From Alzheimer’s disease phospholipase C-gamma-2 (PLCG2) protective variant is a functional hypermorph (2019) · cites this paper as [14]
In the citing paper
“In different models of PLCG2 depletion, homozygous knockout embryos were found to have significant subcutaneous hemorrhaging, suggesting impacted vascular development and bleeding that may underlie embryonic death and reduced frequencies at weaning.”
From PLCG2 modulates TREM2 expression and signaling in response to Alzheimer's disease pathology (2025) · cites this paper as [19]
In the citing paper
“PLCγ2, highly expressed in hematopoietic cells, has the key role in signalling downstream of ITAM-associated receptors; for example, it controls multiple functions of B cells, and several types of innate immune cells in response to stimulation of the B-cell antigen receptor (BCR) and Fc receptors (FcRs), respectively [41,42].”
From Phosphatidylinositol(4,5)bisphosphate: diverse functions at the plasma membrane (2020) · cites this paper as [41]
In the citing paper
“Unlike the germline deletion of PLCγ2 that results in embryonic lethality, mice lacking PLCγ2 enzymatic activity were viable, but with profound defects in B cell development and function. These mice exhibited reduced mature B cells, disrupted differentiation of pro-B cells, and a lack of B1 B cells (24).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“Indeed, PLCγ2-deficient and inducible PLCγ2−/− mice have been widely shown to lack the ability to respond to antigens (24, 26, 27, 28).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“Inducible KO mice showed T cell development and T cell receptor (TCR)-mediated proliferation were normal in the absence of PLCγ2 (24, 26), with development instead depending on the closely related family member PLCγ1 (60).”
From The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration (2021) · cites this paper as [24]
In the citing paper
“On the other hand, PLCγ2 is more broadly present in myeloid cells [5, 25, 26], neutrophils [25, 27], mast cells [25], NK cells [5, 25], B-cells and platelets [5, 28, 29]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“These proteins are critical for the proper maturation, maintenance and function of a range of immune and hematopoietic-lineage cells [5, 23].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“PLCγ2 is expressed in cells of the hematopoietic lineage [5].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“In these cells, PLCγ2, downstream of B-cell receptor and Fc receptor signalling, regulates calcium-dependent functions supporting immune and inflammatory responses [5, 28].”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“the deficits in B-cell development and function are the more pronounced effects described to date”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“PLCγ2-deficient mice are viable, but exhibit haemorrhaging in various organs in addition to severe immunodeficiency [5]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“These include completely ablated calcium responses downstream of the B-cell receptor, affecting the ability to respond to stimuli, and reduced antibody production [5]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
In the citing paper
“In both humans and mice, PLCγ2 loss, as well as strong GOF, mostly results in detrimental and sometimes overlapping phenotypes, as largely described for the peripheral immune system [5, 25]”
From TREM2/PLCγ2 signalling in immune cells: function, structural insight, and potential therapeutic modulation (2021) · cites this paper as [5]
Citations
Cites
Signal transduction by lymphocyte antigen receptors
Weiss, A., & Littman, D. R. (1994) · Cell · doi:10.1016/0092-8674(94)90334-4 · Cited by 2,076
Lymphocyte responses and cytokines
Paul, W. E., & Seder, R. A. (1994) · Cell · doi:10.1016/0092-8674(94)90332-8 · Cited by 1,832
Regulation of Phosphoinositide-Specific Phospholipase C
Rhee, S. G. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.281 · Cited by 1,628
Vetrie, D. L. P., Vořechovský, I., Sideras, P., Holland, J., Davies, A. F., Flinter, F. A., Hammarström, L. L. G., Kinnon, C., Levinsky, R. J., Bobrow, M., et al. (1993) · Nature · doi:10.1038/361226a0 · Cited by 1,465
Deficient expression of a B cell cytoplasmic tyrosine kinase in human X-linked agammaglobulinemia
Tsukada, S., Saffran, D. C., Rawlings, D. J., Parolini, O., Allen, R. C., Klisak, I. J., Sparkes, R. S., Kubagawa, H., Mohandas, T. K., Quan, S. G., et al. (1993) · Cell · doi:10.1016/0092-8674(93)90667-f · Cited by 1,326
Signalling through the lipid products of phosphoinositide-3-OH kinase
Toker, A., & Cantley, L. C. (1997) · Nature · doi:10.1038/42648 · Cited by 1,306
Teglund, S., McKay, C., Schuetz, E. G., van Deursen, J. M., Stravopodis, D. J., Wang, D., Brown, M. P., Bodner, S. M., Grosveld, G. C., & Ihle, J. N. (1998) · Cell · doi:10.1016/s0092-8674(00)81444-0 · Cited by 1,266
Self-citationRothe, J., Lesslauer, W., Loetscher, H., Lang, Y., Koebel, P., Köntgen, F., Althage, A., Zinkernagel, R. M., Steinmetz, M., & Bluethmann, H. (1993) · Nature · doi:10.1038/364798a0 · Cited by 1,246
Daëron, M. (1997) · Annual Review of Immunology · doi:10.1146/annurev.immunol.15.1.203 · Cited by 1,227
Ihle, J. N. (1995) · Nature · doi:10.1038/377591a0 · Cited by 1,201
Self-citation
Cited by
Sorted by citations
Items 101–200 of 476
Chemokines integrate JAK/STAT and G‐protein pathways during chemotaxis and calcium flux responses
Soriano, S. F., Serrano, A., Hernanz‐Falcón, P., de Ana, A. M., Monterrubio, M., Martínez‐A, C., Rodrı́guez-Frade, J. M., & Mellado, M. (2003) · European Journal of Immunology · doi:10.1002/eji.200323897 · Cited by 115
The role of PLCγ2 in immunological disorders, cancer, and neurodegeneration
Jackson, J. T., Mulazzani, E., Nutt, S. L., & Masters, S. L. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100905 · Cited by 113
“As expected, BCR stimulation failed to induce calcium flux or mitogenic stimulation of proliferation in B cells and serum immunoglobulin (Ig) M, G2a, and G3 and T cell–independent antibody production was reduced in the absence of PLCγ2 function (24).”
BackgroundInfluentialB Cell Signaling and Tumorigenesis
Jumaa, H., Hendriks, R. W., & Reth, M. G. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115606 · Cited by 109
Diacylglycerol kinases in immune cell function and self‐tolerance
Zhong, X., Guo, R., Zhou, H., Liu, C., & Wan, E. C. K. (2008) · Immunological Reviews · doi:10.1111/j.1600-065x.2008.00647.x · Cited by 112
Regulation of peripheral B cell maturation
Thomas, M., Srivastava, B., & Allman, D. (2006) · Cellular Immunology · doi:10.1016/j.cellimm.2006.04.007 · Cited by 113
Regulation of B cell fates by BCR signaling components
Kurosaki, T. (2002) · Current Opinion in Immunology · doi:10.1016/s0952-7915(02)00344-8 · Cited by 106
Murugappan, S., Tuluc, F., Dorsam, R. T., Shankar, H., & Kunapuli, S. P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306960200 · Cited by 106
Inherited traits affecting platelet function
Salles, I. I., Feys, H. B., Iserbyt, B. F., Meyer, S. F. D., Vanhoorelbeke, K., & Deckmyn, H. (2008) · Blood Reviews · doi:10.1016/j.blre.2007.11.002 · Cited by 106
Mangin, P., Yuan, Y., Goncalves, I., Eckly, A. E., Freund, M., Cazenave, J., Gachet, C., Jackson, S. P., & Lanza, F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302333200 · Cited by 106
Tkaczyk, C., Beaven, M. A., Brachman, S. M., Metcalfe, D. D., & Gilfillan, A. M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301350200 · Cited by 106
Humphries, L. A., Dangelmaier, C., Sommer, K., Kipp, K. R., Kato, R. M., Griffith, N., Bakman, I., Turk, C. W., Daniel, J. L., & Rawlings, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311985200 · Cited by 104
Tan, J. E.-L., Wong, S. C., Gan, S. K., Xu, S., & Lam, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010800200 · Cited by 101
Tec kinases: modulators of lymphocyte signaling and development
Lewis, C. M., Broussard, C., Czar, M. J., & Schwartzberg, P. L. (2001) · Current Opinion in Immunology · doi:10.1016/s0952-7915(00)00221-1 · Cited by 101
The physiological roles of primary phospholipase C
Yang, Y. R., Follo, M. Y., Cocco, L., & Suh, P. (2013) · Advances in Biological Regulation · doi:10.1016/j.jbior.2013.08.003 · Cited by 104
TLR4 signals in B lymphocytes are transduced via the B cell antigen receptor and SYK
Schweighoffer, E., Nys, J. A., Vanes, L., Smithers, N. N., & Tybulewicz, V. L. J. (2017) · The Journal of Experimental Medicine · doi:10.1084/jem.20161117 · Cited by 107
Phospholipase Cγ2 is necessary for separation of blood and lymphatic vasculature in mice
Ichise, H., Ichise, T., Ohtani, O., & Yoshida, N. (2009) · Development · doi:10.1242/dev.025353 · Cited by 98
The cup runneth over: lessons from the ever-expanding pool of primary immunodeficiency diseases
Milner, J. D., & Holland, S. M. (2013) · Nature reviews. Immunology · doi:10.1038/nri3493 · Cited by 104
Negative Signaling in Fc Receptor Complexes
Daëron, M., & Lesourne, R. (2006) · Advances in immunology · doi:10.1016/s0065-2776(05)89002-9 · Cited by 97
Suzuki‐Inoue, K., Inoue, O., Frampton, J., & Watson, S. P. (2003) · Blood · doi:10.1182/blood-2003-01-0029 · Cited by 97
Evaluation of the role of platelet integrins in fibronectin‐dependent spreading and adhesion
McCarty, O. J. T., Zhao, Y., Andrew, N., Machesky, L. M., Staunton, D., Frampton, J., & Watson, S. P. (2004) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2004.00925.x · Cited by 97
A guide to murine platelet structure, function, assays, and genetic alterations
Jiroušková, M., Shet, A. S., & JOHNSON, G. J. (2007) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2007.02407.x · Cited by 105
Watanabe, N. (2003) · Blood · doi:10.1182/blood-2002-11-3327 · Cited by 95
Nonne, C., Lenain, N., Hechler, B., Mangin, P., Cazenave, J., Gachet, C., & Lanza, F. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000163184.02484.69 · Cited by 95
New insights into the haemostatic function of platelets
Wei, A. H., Schoenwaelder, S. M., Andrews, R. K., & Jackson, S. P. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07819.x · Cited by 94
Cutting Edge Commentary: Origins of B-1 Cells
Wortis, H. H., & Berland, R. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.4.2163 · Cited by 92
Munnix, I. C. A., Strehl, A., Kuijpers, M. J. E., Auger, J. M., van der Meijden, P. E. J., van Zandvoort, M. A. M. J., Egbrink, M. G. A. O., Nieswandt, B., & Heemskerk, J. W. M. (2005) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000193568.71980.4a · Cited by 91
Functional Dichotomy in Natural Killer Cell Signaling
Colucci, F., Rosmaraki, E. E., Bregenholt, S., Samson, S., Bartolo, V. D., Turner, M., Vanes, L., Tybulewicz, V. L. J., & Santo, J. P. D. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.12.1413 · Cited by 90
Tyrosine Residues in Phospholipase Cγ2 Essential for the Enzyme Function in B-cell Signaling
Rodriguez, R., Matsuda, M., Perišić, O., Bravo, J., Paul, A., Jones, N. P., Light, Y., Swann, K., Williams, R. L., & Katan, M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107577200 · Cited by 90
Stadtmann, A., Brinkhaus, L., Mueller, H., Rossaint, J., Bolomini‐Vittori, M., Bergmeier, W., Aken, H. V., Wagner, D. D., Laudanna, C., Ley, K. F., et al. (2011) · European Journal of Immunology · doi:10.1002/eji.201041196 · Cited by 94
Phospholipase C families: Common themes and versatility in physiology and pathology
Katan, M., & Cockcroft, S. (2020) · Progress in Lipid Research · doi:10.1016/j.plipres.2020.101065 · Cited by 89
Pandey, V., Mihara, S., Fensome, A. C., Bolsover, S. R., & Cockcroft, S. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.7.4048 · Cited by 88
Deason-Towne, F., Perraud, A., & Schmitz, C. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.06.015 · Cited by 88
Bertozzi, C. C., Hess, P. R., & Kahn, M. L. (2010) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.110.217281 · Cited by 88
PLAID: a Syndrome of Complex Patterns of Disease and Unique Phenotypes
Milner, J. D. (2015) · Journal of Clinical Immunology · doi:10.1007/s10875-015-0177-x · Cited by 85
The SLP-76 family of adapter proteins
Wu, J. N., & Koretzky, G. A. (2004) · Seminars in Immunology · doi:10.1016/j.smim.2004.08.018 · Cited by 87
Bam32 Links the B Cell Receptor to ERK and JNK and Mediates B Cell Proliferation but Not Survival
Han, A. S., Saijo, K., Mecklenbräuker, I., Tarakhovsky, A., & Nussenzweig, M. C. (2003) · Immunity · doi:10.1016/s1074-7613(03)00275-9 · Cited by 84
Integrin αIIbβ3-dependent Calcium Signals Regulate Platelet-Fibrinogen Interactions under Flow
Goncalves, I., Hughan, S. C., Schoenwaelder, S. M., Yap, C. L., Yuan, Y., & Jackson, S. P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306504200 · Cited by 84
Manne, B. K., Badolia, R., Dangelmaier, C., Eble, J. A., Ellmeier, W., Kahn, M. L., & Kunapuli, S. P. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.629527 · Cited by 82
CD8+ T Cells Regulate Bone Tumor Burden Independent of Osteoclast Resorption
Zhang, K., Kim, S., Cremasco, V., Hirbe, A. C., Novack, D. V., Weilbaecher, K. N., & Faccio, R. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3922 · Cited by 82
Cho, M. J., Liu, J., Pestina, T. I., Steward, S. A., Thomas, D. W., Coffman, T. M., Wang, D., Jackson, C. W., & Gartner, T. K. (2003) · Blood · doi:10.1182/blood-2002-05-1363 · Cited by 82
Self-citationDütting, S., Brachs, S., & Mielenz, D. (2011) · Cell Communication and Signaling · doi:10.1186/1478-811x-9-2 · Cited by 80
Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509396200 · Cited by 80
Liu, J., Pestina, T. I., Berndt, M. C., Jackson, C. W., & Gartner, T. K. (2005) · Blood · doi:10.1182/blood-2005-04-1667 · Cited by 80
Self-citationCapietto, A.-H., Kim, S., Sanford, D. E., Linehan, D. C., Hikida, M., Kumosaki, T., Novack, D. V., & Faccio, R. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130281 · Cited by 79
Itk Phosphorylation Sites Are Required for Functional Activity in Primary T Cells
Wilcox, H. M., & Berg, L. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304811200 · Cited by 80
HLA and kidney disease: from associations to mechanisms
Robson, K. J., Ooi, J. D., Holdsworth, S. R., Rossjohn, J., & Kitching, A. R. (2018) · Nature Reviews Nephrology · doi:10.1038/s41581-018-0057-8 · Cited by 79
Gupta, S., Konradt, C., Corken, A. L., Ware, J. L., Nieswandt, B., Paola, J. D., Yu, M., Wang, D., Nieman, M. T., Whiteheart, S. W., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2007642117 · Cited by 78
Self-citationPerraud, A. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2004.04.013 · Cited by 77
Martínez‐Torres, A. C., Quiney, C., Attout, T., Boullet, H., Herbi, L., Vela, L., Barbier, S., Château, D., Chapiro, É., Nguyen‐Khac, F., et al. (2015) · PLoS Medicine · doi:10.1371/journal.pmed.1001796 · Cited by 84
HIV-1 Nef Interacts with Inositol Trisphosphate Receptor to Activate Calcium Signaling in T Cells
Manninen, A., & Saksela, K. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20012039 · Cited by 76
Matsuda, M., Paterson, H. F., Rodriguez, R., Fensome, A. C., Ellis, M. V., Swann, K., & Katan, M. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.153.3.599 · Cited by 74
A Bayesian extension of the hypergeometric test for functional enrichment analysis
Cao, J., & Zhang, S. (2013) · Biometrics · doi:10.1111/biom.12122 · Cited by 75
Németh, T., Futosi, K., Sitaru, C., Ruland, J., & Mócsai, A. (2016) · Nature Communications · doi:10.1038/ncomms11004 · Cited by 74
PECAM-1 negatively regulates GPIb/V/IX signaling in murine platelets
Rathore, V., Stapleton, M. A., Hillery, C. A., Montgomery, R. R., Nichols, T. C., Merricks, E. P., Newman, D. K., & Newman, P. J. (2003) · Blood · doi:10.1182/blood-2003-06-1888 · Cited by 75
Strategies of Natural Killer Cell Recognition and Signaling
Stewart, C. A., Vivier, É., & Colonna, M. (2005) · Current topics in microbiology and immunology · doi:10.1007/3-540-27743-9_1 · Cited by 74
Boisson, B., Quartier, P., & Casanova, J. (2015) · Current Opinion in Immunology · doi:10.1016/j.coi.2015.01.005 · Cited by 75
Lymphatic Vasculature Development
Oliver, G. C., & Srinivasan, R. S. (2008) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1413.006 · Cited by 74
PLC-γ2 is essential for formation and maintenance of memory B cells
Hikida, M., Casola, S., Takahashi, N., Kaji, T., Takemori, T., Rajewsky, K., & Kurosaki, T. (2009) · Journal of Experimental Medicine · doi:10.1084/jem.20082100 · Cited by 73
The Biochemistry and Biology of BAFF, APRIL and Their Receptors
Kalled, S. L., Ambrose, C. M., & Hsu, Y. (2004) · KARGER eBooks · doi:10.1159/000082105 · Cited by 73
IL-10-producing regulatory B cells and plasmocytes: Molecular mechanisms and disease relevance
Cerqueira, C., Manfroi, B., & Fillatreau, S. (2019) · Seminars in Immunology · doi:10.1016/j.smim.2019.101323 · Cited by 74
Fujimoto, M., Poe, J. C., Hasegawa, M., & Tedder, T. F. (2000) · Immunologic Research · doi:10.1385/ir:22:2-3:281 · Cited by 72
Foerster, C., Voelxen, N., Rakhmanov, M., Keller, B., Gutenberger, S., Goldacker, S., Thiel, J., Feske, S., Peter, H., & Warnatz, K. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000434 · Cited by 72
Diverging signaling events control the pathway of GPVI down-regulation in vivo
Rabie, T., Varga-Szabó, D., Bender, M., Pozgaj, R., Lanza, F., Saito, T., Watson, S. P., & Nieswandt, B. (2007) · Blood · doi:10.1182/blood-2006-11-058107 · Cited by 72
Phospholipase Cγ2 Is Essential for Specific Functions of FcεR and FcγR
Wen, R., Jou, S.-T., Chen, Y., Hoffmeyer, A., & Wang, D. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.12.6743 · Cited by 71
Self-citationThe Isoforms of Phospholipase C-γ Are Differentially Used by Distinct Human NK Activating Receptors
Upshaw, J. L., Schoon, R. A., Dick, C. J., Billadeau, D. D., & Leibson, P. J. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.1.213 · Cited by 70
Role of Calcium Signaling in B Cell Activation and Biology
Baba, Y., & Kurosaki, T. (2015) · Current topics in microbiology and immunology · doi:10.1007/82_2015_477 · Cited by 72
Non-receptor protein tyrosine kinases
Tsygankov, A. Y. (2003) · Frontiers in bioscience · doi:10.2741/1106 · Cited by 72
Yablonski, D., & Weiss, A. (2001) · Advances in immunology · doi:10.1016/s0065-2776(01)79003-7 · Cited by 65
Matalon, O., Fried, S., Ben‐Shmuel, A., Pauker, M. H., Joseph, N., Keizer, D., Piterburg, M., & Barda‐Saad, M. (2016) · Science Signaling · doi:10.1126/scisignal.aad6182 · Cited by 72
PI3K signaling controls cell fate at many points in B lymphocyte development and activation
Donahue, A. C., & Fruman, D. A. (2004) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2003.12.024 · Cited by 68
Mechanism of Tyrosine Phosphorylation and Activation of Phospholipase C-γ1
Sekiya, F., Poulin, B., Kim, Y. J., & Rhee, S. G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m405116200 · Cited by 66
Marafioti, T. (2003) · Blood · doi:10.1182/blood-2003-05-1487 · Cited by 67
Lipid Signaling in T-Cell Development and FunctionPreprint
Huang, Y. H., & Sauer, K. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a002428 · Cited by 68
Regulation of NK Cell-Mediated Cytotoxicity by the Adaptor Protein 3BP2
Jevremović, D., Billadeau, D. D., Schoon, R. A., Dick, C. J., & Leibson, P. J. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.12.7219 · Cited by 65
Enhanced T Cell Proliferation in Mice Lacking the p85β Subunit of Phosphoinositide 3-Kinase
Deane, J. A., Trifilo, M. J., Yballe, C. M., Choi, S., Lane, T. E., & Fruman, D. A. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.11.6615 · Cited by 65
Magno, L., Bunney, T. D., Mead, E., Svensson, F., & Bictash, M. N. (2021) · Molecular Neurodegeneration · doi:10.1186/s13024-021-00436-5 · Cited by 64
Suzuki‐Inoue, K., Wilde, J. I., Andrews, R. K., Auger, J. M., Siraganian, R. P., Sekiya, F., Rhee, S. G., & Watson, S. P. (2004) · Biochemical Journal · doi:10.1042/bj20031430 · Cited by 64
Epple, H., Cremasco, V., Zhang, K., Mao, D., Longmore, G. D., & Faccio, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00259-08 · Cited by 64
Characterization of Phospholipase Cγ Enzymes with Gain-of-Function Mutations
Everett, K. L., Bunney, T. D., Yoon, Y., Rodrigues-Lima, F., Harris, R., Driscoll, P. C., Abe, K., Fuchs, H., Hrabé de Angelis, M., Yu, P., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.019265 · Cited by 63
ENU-mutagenesis: insight into immune function and pathology
Cook, M., Vinuesa, C. G., & Goodnow, C. C. (2006) · Current Opinion in Immunology · doi:10.1016/j.coi.2006.07.011 · Cited by 62
Matalon, O., Ben‐Shmuel, A., Kivelevitz, J., Sabag, B., Fried, S., Joseph, N., Noy, E., Biber, G., & Barda‐Saad, M. (2018) · The EMBO Journal · doi:10.15252/embj.201696264 · Cited by 59
The adaptor protein shc is involved in the negative regulation of NK cell-mediated cytotoxicity
Galandrini, R., Tassi, I., Morrone, S., Lanfrancone, L., Pelicci, P. G., Piccoli, M., Frati, L., & Santoni, A. (2001) · European Journal of Immunology · doi:10.1002/1521-4141(200107)31:7 · Cited by 32
Coupling Between B Cell Receptor and Phospholipase C-γ2 Is Essential for Mature B Cell Development
Hikida, M., Johmura, S., Hashimoto, A., Takezaki, M., & Kurosaki, T. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20030280 · Cited by 62
Novel Igα (CD79a) gene mutation in a Turkish patient with B cell‐deficient agammaglobulinemia
Wang, Y., Kanegane, H., Sanal, Ö., Tezcan, İ., Ersoy, F., Futatani, T., & Miyawaki, T. (2002) · American Journal of Medical Genetics · doi:10.1002/ajmg.10296 · Cited by 62
Activation of Phospholipase Cγ2 by Tyrosine Phosphorylation
Özdener, F., Dangelmaier, C., Ashby, B., Kunapuli, S. P., & Daniel, J. L. (2002) · Molecular Pharmacology · doi:10.1124/mol.62.3.672 · Cited by 60
Rho GTPase Cdc42 is essential for B-lymphocyte development and activation
Guo, F., Velu, C. S., Grimes, H. L., & Zheng, Y. (2009) · Blood · doi:10.1182/blood-2009-04-214676 · Cited by 63
The identification of novel PLC-γ inhibitors using virtual high throughput screening
Reynisson, J., Court, W. J., O’Neill, C., Day, J. E. H., Patterson, L., McDonald, E., Workman, P., Katan, M., & Eccles, S. A. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.02.049 · Cited by 58
Kim, J., Cheon, Y., Oh, H. M., Rho, M., Erkhembaatar, M., Kim, M. S., Lee, C. H., Kim, J. J., Choi, M. K., Yoon, K., et al. (2013) · Bone · doi:10.1016/j.bone.2013.12.013 · Cited by 59
Takenaka, K., Fukami, K., Otsuki, M., Nakamura, Y., Kataoka, Y., Wada, M., Tsuji, K., Nishikawa, S.-I., Yoshida, N., & Takenawa, T. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.20.7329-7338.2003 · Cited by 58
Phosphorylation of Tyr342 in the Linker Region of Syk Is Critical for FcεRI Signaling in Mast Cells
Zhang, J., Berenstein, E. H., & Siraganian, R. P. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.23.8144-8154.2002 · Cited by 58
Quinton, T. M., Özdener, F., Dangelmaier, C., Daniel, J. L., & Kunapuli, S. P. (2002) · Blood · doi:10.1182/blood.v99.9.3228 · Cited by 57
Martín-Nalda, A., Fortuny, C., Rey, L., Bunney, T. D., Alsina, L., Esteve-Solé, A., Bull, D., Anton, M. C., Basagaña, M., Casals, F., et al. (2020) · Journal of Clinical Immunology · doi:10.1007/s10875-020-00794-7 · Cited by 56
“PLCG2 was proposed as a good candidate gene to explain some B cell deficiencies in humans because the mouse model of PLCγ2 deficiency showed a decrease of mature B cell and a block in the pro-B cell differentiation [22].”
BackgroundJou, S., Chien, Y., Yang, Y., Wang, T. ‐., Shyur, S., Chou, C. ‐., Chang, M., Lin, D., Lin, K., & Chiang, B. (2006) · International Journal of Immunogenetics · doi:10.1111/j.1744-313x.2006.00627.x · Cited by 56
Walliser, C., Retlich, M., Harris, R., Everett, K. L., Josephs, M. B., Vatter, P., Esposito, D., Driscoll, P. C., Katan, M., Gierschik, P., et al. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803316200 · Cited by 56
Glassford, J., Soeiro, I., Skarell, S. M., Banerji, L., Holman, M. J., Klaus, G. G. B., Kadowaki, T., Koyasu, S., & Lam, E. W. ‐. (2003) · Oncogene · doi:10.1038/sj.onc.1206425 · Cited by 56
The Role of BANK1 in B Cell Signaling and Disease
Hernández, G. G., Morell, M. H., & Alarcón-Riquelme, M. E. (2021) · Cells · doi:10.3390/cells10051184 · Cited by 55
Matsumoto, M., Oyamada, K., Takahashi, H., Sato, T., Hatakeyama, S., & Nakayama, K. I. (2009) · PROTEOMICS · doi:10.1002/pmic.200900011 · Cited by 54
Moreno-García, M. E., López-Bojórques, L. N., Zentella, A., Humphries, L. A., Rawlings, D. J., & Santos-Argumedo, L. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.5.2687 · Cited by 54
PLCγ-dependent mTOR signalling controls IL-7-mediated early B cell development
Yu, M., Chen, Y., Zeng, H., Zheng, Y., Fu, G., Zhu, W., Broeckel, U., Aggarwal, P., Turner, A., Neale, G. A. M., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01388-5 · Cited by 55
Self-citationMiosge, L. A., Blasioli, J., Bléry, M., & Goodnow, C. C. (2002) · The Journal of Experimental Medicine · doi:10.1084/jem.20020959 · Cited by 53
Metadata
- Authors
- Wang, D., Feng, J., Wen, R., Marine, J.-C., Sangster, M. Y., Parganas, E., Hoffmeyer, A., Jackson, C. W., Cleveland, J. L., Murray, P. J., & Ihle, J. N.
- Affiliations
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Ihle, James N.
- ORCID
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2000-07
- Volume
- 13
- Issue
- 1
- Pages
- 25-35
- ISSN
- 1074-7613 (ISSN-L)
- OpenAlex
- W2039490597
- Cited by
- 475
- References
- 54
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 5 · 2023: 12 · 2022: 4 · 2021: 13 · 2020: 11 · 2019: 10 · 2018: 6 · 2017: 10 · 2016: 12 · 2015: 16 · 2014: 12 · 2013: 14 · 2012: 16
- FWCI
- 12.85
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (P01HL053749, P01HL53749)
- National Cancer Institute (CA21765, P30CA021765)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01-DK42932, R01DK042932)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
- Life Sciences › Immunology and Microbiology › Immunology › Immunodeficiency and Autoimmune Disorders
- Life Sciences › Immunology and Microbiology › Immunology › Monoclonal and Polyclonal Antibodies Research
- Keywords
- PLCγ2, B cell development, calcium flux, BTK signaling, 2B4, immunoglobulin superfamily receptors, platelet aggregation
- MeSH terms
- Agammaglobulinaemia Tyrosine Kinase, Animals, B-Lymphocytes, Blood Platelets, Carrier Proteins, Hematopoiesis, Isoenzymes, Mice, Inbred C57BL, Type C Phospholipases, Phosphoproteins, Protein-Tyrosine Kinases, Receptors, Antigen, B-Cell, Receptors, IgG, Mice, Knockout, Adaptor Proteins, Signal Transducing, Mice, Phospholipase C gamma
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review